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Entry version 194 (25 May 2022)
Sequence version 1 (01 Nov 1999)
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Protein

Lysyl oxidase homolog 2

Gene

LOXL2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine) (PubMed:27735137).

Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation (PubMed:27735137).

Shows no activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2) (PubMed:27735137).

Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription (PubMed:25959397).

LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency including POU5F1/OCT4, NANOG, KLF4 and SOX2 (By similarity).

Involved in epithelial to mesenchymal transition (EMT) via interaction with SNAI1 and participates in repression of E-cadherin CDH1, probably by mediating deamination of histone H3 (PubMed:16096638, PubMed:27735137, PubMed:24414204).

During EMT, involved with SNAI1 in negatively regulating pericentromeric heterochromatin transcription (PubMed:24239292).

SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits (PubMed:24239292).

Interacts with the endoplasmic reticulum protein HSPA5 which activates the IRE1-XBP1 pathway of the unfolded protein response, leading to expression of several transcription factors involved in EMT and subsequent EMT induction (PubMed:28332555).

Involved in E-cadherin repression following hypoxia, a hallmark of EMT believed to amplify tumor aggressiveness, suggesting that it may play a role in tumor progression (PubMed:20026874).

When secreted into the extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin (PubMed:20306300).

Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding (PubMed:21835952).

Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation (By similarity).

By similarity8 Publications

Miscellaneous

Its overexpression in a number of cancers and its ability to promote epithelial to mesenchymal transition suggest that LOXL2 might play a role in tumor progression: expression is correlated with metastasis and decreased survival in patients with aggressive breast cancer (PubMed:21233336, PubMed:21732535). Allosteric inhibition by AB0023 inhibits formation of the tumor microenvironment and reduces metastatic tumor burden in xenograft models (PubMed:20818376, PubMed:21732535). However, inhibiting the enzyme activity of LOXL2 may not be sufficient, since inhibition of keratinocyte differentiation is not prevented in mutants that lack enzyme activity nor by inhibition of activity by the AB0023 antibody, thereby promoting development of squamous cell carcinomas (PubMed:22157764).4 Publications

Caution

The original paper reporting the role of LOXL2 in deamination of trimethylated 'Lys-4' of histone H3 was retracted due to inappropriate manipulation of figure data (PubMed:22483618, PubMed:27392148). However, this role was confirmed in a subsequent publication (PubMed:27735137).2 Publications1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

According to some reports, it is inhibited by beta-aminopropionitrile (BAPN) (PubMed:20439985 and PubMed:23319596). According to another report, it is not inhibited by beta-aminopropionitrile (BAPN) (PubMed:20306300). Specifically inhibited by a mouse monoclonal antibody AB0023, inhibition occurs in a non-competitive manner.4 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 2.04 min(-1) with tropoelastin as substrate (without the first three SRCR domains). kcat is 0.62 min(-1) with tropoelastin as substrate (without all four SRCR domains).
  1. KM=1.01 mM for 1,5-diaminopentane2 Publications
  2. KM=1.05 mM for spermine2 Publications
  3. KM=0.59 µM for tropoelastin (without the first three SRCR domains)2 Publications
  4. KM=0.62 µM for tropoelastin (without all four SRCR domains)2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi549Calcium1 Publication1
Metal bindingi550Calcium; via carbonyl oxygen1 Publication1
Metal bindingi626Copper1 Publication1
Metal bindingi628Copper1 Publication1
Metal bindingi630Copper1 Publication1
Metal bindingi722Calcium1 Publication1
Metal bindingi724Calcium; via carbonyl oxygen1 Publication1
Metal bindingi727Calcium1 Publication1
Metal bindingi728Calcium1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChromatin regulator, Oxidoreductase, Repressor
Biological processTranscription, Transcription regulation
LigandCalcium, Copper, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.4.3.13, 2681

Pathway Commons web resource for biological pathway data

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PathwayCommonsi
Q9Y4K0

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1566948, Elastic fibre formation
R-HSA-2243919, Crosslinking of collagen fibrils

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q9Y4K0

SIGNOR Signaling Network Open Resource

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SIGNORi
Q9Y4K0

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Lysyl oxidase homolog 2 (EC:1.4.3.134 Publications)
Alternative name(s):
Lysyl oxidase-like protein 2
Lysyl oxidase-related protein 2
Lysyl oxidase-related protein WS9-14
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:LOXL2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 8

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:6666, LOXL2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
606663, gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q9Y4K0

Eukaryotic Pathogen, Vector and Host Database Resources

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VEuPathDBi
HostDB:ENSG00000134013

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Basement membrane, Chromosome, Endoplasmic reticulum, Extracellular matrix, Nucleus, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi455N → Q: Inhibits secretion. 1 Publication1
Mutagenesisi626 – 628HRH → ARA: Abolishes oxidase activity and oxidation of trimethylated 'Lys-4' of histone H3 but does not affect secretion, interaction with SNAI1, binding to the CDH1 promoter, repression of CDH1 transcription or ability to induce EMT. 2 Publications3
Mutagenesisi626H → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi628H → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi630H → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi644N → Q: Inhibits secretion. 1 Publication1
Mutagenesisi653K → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi689Y → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi689Y → F: Does not affect ability to inhibit keratinocyte differentiation. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
4017

Open Targets

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OpenTargetsi
ENSG00000134013

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA30429

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
Q9Y4K0, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3714029

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2853

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
LOXL2

Domain mapping of disease mutations (DMDM)

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DMDMi
13878585

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 25Sequence analysisAdd BLAST25
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001853226 – 774Lysyl oxidase homolog 2Add BLAST749

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi84 ↔ 148PROSITE-ProRule annotation
Disulfide bondi97 ↔ 158PROSITE-ProRule annotation
Disulfide bondi128 ↔ 138PROSITE-ProRule annotation
Disulfide bondi218 ↔ 291PROSITE-ProRule annotation
Disulfide bondi231 ↔ 301PROSITE-ProRule annotation
Disulfide bondi265 ↔ 275PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi288N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi351 ↔ 414PROSITE-ProRule annotation
Disulfide bondi364 ↔ 424PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi395 ↔ 405PROSITE-ProRule annotationCombined sources1 Publication
Glycosylationi455N-linked (GlcNAc...) (complex) asparagine1 Publication1
Disulfide bondi464 ↔ 530PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi477 ↔ 543PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi511 ↔ 521PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi573 ↔ 625Combined sources1 Publication
Disulfide bondi579 ↔ 695Combined sources1 Publication
Glycosylationi644N-linked (GlcNAc...) (complex) asparagineCombined sources2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki653 ↔ 689Lysine tyrosylquinone (Lys-Tyr)2 Publications
Disulfide bondi657 ↔ 673Combined sources1 Publication
Disulfide bondi663 ↔ 685Combined sources1 Publication
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei6892',4',5'-topaquinone1 Publication1
Disulfide bondi732 ↔ 746PROSITE-ProRule annotationCombined sources1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine.2 Publications
N-glycosylated. N-glycosylation on Asn-455 and Asn-644 may be essential for proper folding and secretion; may be composed of a fucosylated carbohydrates attached to a trimannose N-linked glycan core.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, LTQ, TPQ

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q9Y4K0

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9Y4K0

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q9Y4K0

MaxQB - The MaxQuant DataBase

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MaxQBi
Q9Y4K0

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q9Y4K0

PeptideAtlas

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PeptideAtlasi
Q9Y4K0

PRoteomics IDEntifications database

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PRIDEi
Q9Y4K0

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
86223

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
1480, 1 N-Linked glycan (1 site)

GlyGen: Computational and Informatics Resources for Glycoscience

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GlyGeni
Q9Y4K0, 3 sites, 1 N-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9Y4K0

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q9Y4K0

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in many tissues (PubMed:10212285). Highest expression in reproductive tissues, placenta, uterus and prostate (PubMed:10212285). In esophageal epithelium, expressed in the basal, prickle and granular cell layers (PubMed:22204712). Up-regulated in a number of cancers cells and tissues.2 Publications

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Strongly induced in hypoxia. Direct transcriptional target of HIF1A.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000134013, Expressed in stromal cell of endometrium and 194 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9Y4K0, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9Y4K0, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000134013, Tissue enhanced (smooth)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of some chromatin repressor complex.

Interacts with SNAI1 (PubMed:16096638).

Interacts with TAF10 (PubMed:25959397).

Interacts with HSPA5 (PubMed:28332555).

Interacts with EFEMP2 (PubMed:27339457).

4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
110201, 113 interactors

Protein interaction database and analysis system

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IntActi
Q9Y4K0, 34 interactors

Molecular INTeraction database

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MINTi
Q9Y4K0

STRING: functional protein association networks

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STRINGi
9606.ENSP00000373783

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q9Y4K0

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
Q9Y4K0, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1774
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

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AlphaFoldDBi
Q9Y4K0

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q9Y4K0

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini58 – 159SRCR 1PROSITE-ProRule annotationAdd BLAST102
Domaini188 – 302SRCR 2PROSITE-ProRule annotationAdd BLAST115
Domaini326 – 425SRCR 3PROSITE-ProRule annotationAdd BLAST100
Domaini435 – 544SRCR 4PROSITE-ProRule annotationAdd BLAST110

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni548 – 751Lysyl-oxidase likeAdd BLAST204

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The fourth SRCR domain plays an important role in optimizing the catalytic activity of the lysyl-oxidase like (LOX) catalytic domain.

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the lysyl oxidase family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG502QSX8, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000155874

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_002555_3_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9Y4K0

Identification of Orthologs from Complete Genome Data

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OMAi
YCTGKEA

Database of Orthologous Groups

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OrthoDBi
815466at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9Y4K0

TreeFam database of animal gene trees

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TreeFami
TF326061

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.10.250.10, 4 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001695, Lysyl_oxidase
IPR019828, Lysyl_oxidase_CS
IPR001190, SRCR
IPR017448, SRCR-like_dom
IPR036772, SRCR-like_dom_sf

Pfam protein domain database

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Pfami
View protein in Pfam
PF01186, Lysyl_oxidase, 1 hit
PF00530, SRCR, 4 hits

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00074, LYSYLOXIDASE
PR00258, SPERACTRCPTR

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00202, SR, 4 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56487, SSF56487, 4 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00926, LYSYL_OXIDASE, 1 hit
PS00420, SRCR_1, 2 hits
PS50287, SRCR_2, 4 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 8 potential isoforms that are computationally mapped.Show allAlign All

Q9Y4K0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MERPLCSHLC SCLAMLALLS PLSLAQYDSW PHYPEYFQQP APEYHQPQAP
60 70 80 90 100
ANVAKIQLRL AGQKRKHSEG RVEVYYDGQW GTVCDDDFSI HAAHVVCREL
110 120 130 140 150
GYVEAKSWTA SSSYGKGEGP IWLDNLHCTG NEATLAACTS NGWGVTDCKH
160 170 180 190 200
TEDVGVVCSD KRIPGFKFDN SLINQIENLN IQVEDIRIRA ILSTYRKRTP
210 220 230 240 250
VMEGYVEVKE GKTWKQICDK HWTAKNSRVV CGMFGFPGER TYNTKVYKMF
260 270 280 290 300
ASRRKQRYWP FSMDCTGTEA HISSCKLGPQ VSLDPMKNVT CENGLPAVVS
310 320 330 340 350
CVPGQVFSPD GPSRFRKAYK PEQPLVRLRG GAYIGEGRVE VLKNGEWGTV
360 370 380 390 400
CDDKWDLVSA SVVCRELGFG SAKEAVTGSR LGQGIGPIHL NEIQCTGNEK
410 420 430 440 450
SIIDCKFNAE SQGCNHEEDA GVRCNTPAMG LQKKLRLNGG RNPYEGRVEV
460 470 480 490 500
LVERNGSLVW GMVCGQNWGI VEAMVVCRQL GLGFASNAFQ ETWYWHGDVN
510 520 530 540 550
SNKVVMSGVK CSGTELSLAH CRHDGEDVAC PQGGVQYGAG VACSETAPDL
560 570 580 590 600
VLNAEMVQQT TYLEDRPMFM LQCAMEENCL SASAAQTDPT TGYRRLLRFS
610 620 630 640 650
SQIHNNGQSD FRPKNGRHAW IWHDCHRHYH SMEVFTHYDL LNLNGTKVAE
660 670 680 690 700
GHKASFCLED TECEGDIQKN YECANFGDQG ITMGCWDMYR HDIDCQWVDI
710 720 730 740 750
TDVPPGDYLF QVVINPNFEV AESDYSNNIM KCRSRYDGHR IWMYNCHIGG
760 770
SFSEETEKKF EHFSGLLNNQ LSPQ
Length:774
Mass (Da):86,725
Last modified:November 1, 1999 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9DF5D25D4824BCCD
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 8 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E5RJL2E5RJL2_HUMAN
Lysyl oxidase homolog 2
LOXL2
151Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E5RI22E5RI22_HUMAN
Lysyl oxidase homolog 2
LOXL2
139Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E5RFE2E5RFE2_HUMAN
Lysyl oxidase homolog 2
LOXL2
95Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0YAR1H0YAR1_HUMAN
Lysyl oxidase homolog 2
LOXL2
207Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E5RFY0E5RFY0_HUMAN
Lysyl oxidase homolog 2
LOXL2
258Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E5RHH3E5RHH3_HUMAN
Lysyl oxidase homolog 2
LOXL2
218Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0YAP6H0YAP6_HUMAN
Lysyl oxidase homolog 2
LOXL2
67Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
R4GMS2R4GMS2_HUMAN
Lysyl oxidase homolog 2
LOXL2
101Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAD34343 differs from that shown. Reason: Erroneous termination. Extended C-terminus.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti184E → K in BAG35197 (PubMed:14702039).Curated1
Sequence conflicti239E → G in BAD96197 (Ref. 3) Curated1
Sequence conflicti295L → Q in AAD34343 (PubMed:10212285).Curated1
Sequence conflicti536Q → R in BAG35197 (PubMed:14702039).Curated1
Sequence conflicti652H → Q in AAD34343 (PubMed:10212285).Curated1
Sequence conflicti746C → S in AAD34343 (PubMed:10212285).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_050010359S → W. Corresponds to variant dbSNP:rs4602894Ensembl.1
Natural variantiVAR_024527570M → L2 PublicationsCorresponds to variant dbSNP:rs1063582Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
U89942 mRNA Translation: AAB49697.1
AK312266 mRNA Translation: BAG35197.1
AK222477 mRNA Translation: BAD96197.1
AC090197 Genomic DNA No translation available.
BC000594 mRNA Translation: AAH00594.1
AF117949 mRNA Translation: AAD34343.1 Sequence problems.

The Consensus CDS (CCDS) project

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CCDSi
CCDS34864.1

NCBI Reference Sequences

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RefSeqi
NP_002309.1, NM_002318.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000389131.8; ENSP00000373783.3; ENSG00000134013.16

Database of genes from NCBI RefSeq genomes

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GeneIDi
4017

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:4017

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

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MANE-Selecti
ENST00000389131.8; ENSP00000373783.3; NM_002318.3; NP_002309.1

UCSC genome browser

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UCSCi
uc003xdh.2, human

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89942 mRNA Translation: AAB49697.1
AK312266 mRNA Translation: BAG35197.1
AK222477 mRNA Translation: BAD96197.1
AC090197 Genomic DNA No translation available.
BC000594 mRNA Translation: AAH00594.1
AF117949 mRNA Translation: AAD34343.1 Sequence problems.
CCDSiCCDS34864.1
RefSeqiNP_002309.1, NM_002318.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5ZE3X-ray2.40A/B318-774[»]
AlphaFoldDBiQ9Y4K0
SMRiQ9Y4K0
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi110201, 113 interactors
IntActiQ9Y4K0, 34 interactors
MINTiQ9Y4K0
STRINGi9606.ENSP00000373783

Chemistry databases

BindingDBiQ9Y4K0
ChEMBLiCHEMBL3714029
GuidetoPHARMACOLOGYi2853

PTM databases

GlyConnecti1480, 1 N-Linked glycan (1 site)
GlyGeniQ9Y4K0, 3 sites, 1 N-linked glycan (1 site)
iPTMnetiQ9Y4K0
PhosphoSitePlusiQ9Y4K0

Genetic variation databases

BioMutaiLOXL2
DMDMi13878585

Proteomic databases

EPDiQ9Y4K0
jPOSTiQ9Y4K0
MassIVEiQ9Y4K0
MaxQBiQ9Y4K0
PaxDbiQ9Y4K0
PeptideAtlasiQ9Y4K0
PRIDEiQ9Y4K0
ProteomicsDBi86223

Protocols and materials databases

ABCD curated depository of sequenced antibodies

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ABCDi
Q9Y4K0, 1 sequenced antibody

Antibodypedia a portal for validated antibodies

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Antibodypediai
22758, 474 antibodies from 35 providers

The DNASU plasmid repository

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DNASUi
4017

Genome annotation databases

EnsembliENST00000389131.8; ENSP00000373783.3; ENSG00000134013.16
GeneIDi4017
KEGGihsa:4017
MANE-SelectiENST00000389131.8; ENSP00000373783.3; NM_002318.3; NP_002309.1
UCSCiuc003xdh.2, human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
4017
DisGeNETi4017

GeneCards: human genes, protein and diseases

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GeneCardsi
LOXL2
HGNCiHGNC:6666, LOXL2
HPAiENSG00000134013, Tissue enhanced (smooth)
MIMi606663, gene
neXtProtiNX_Q9Y4K0
OpenTargetsiENSG00000134013
PharmGKBiPA30429
VEuPathDBiHostDB:ENSG00000134013

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG502QSX8, Eukaryota
GeneTreeiENSGT00940000155874
HOGENOMiCLU_002555_3_0_1
InParanoidiQ9Y4K0
OMAiYCTGKEA
OrthoDBi815466at2759
PhylomeDBiQ9Y4K0
TreeFamiTF326061

Enzyme and pathway databases

BRENDAi1.4.3.13, 2681
PathwayCommonsiQ9Y4K0
ReactomeiR-HSA-1566948, Elastic fibre formation
R-HSA-2243919, Crosslinking of collagen fibrils
SignaLinkiQ9Y4K0
SIGNORiQ9Y4K0

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
4017, 9 hits in 1074 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
LOXL2, human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
LOXL2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
4017
PharosiQ9Y4K0, Tchem

Protein Ontology

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PROi
PR:Q9Y4K0
RNActiQ9Y4K0, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000134013, Expressed in stromal cell of endometrium and 194 other tissues
ExpressionAtlasiQ9Y4K0, baseline and differential
GenevisibleiQ9Y4K0, HS

Family and domain databases

Gene3Di3.10.250.10, 4 hits
InterProiView protein in InterPro
IPR001695, Lysyl_oxidase
IPR019828, Lysyl_oxidase_CS
IPR001190, SRCR
IPR017448, SRCR-like_dom
IPR036772, SRCR-like_dom_sf
PfamiView protein in Pfam
PF01186, Lysyl_oxidase, 1 hit
PF00530, SRCR, 4 hits
PRINTSiPR00074, LYSYLOXIDASE
PR00258, SPERACTRCPTR
SMARTiView protein in SMART
SM00202, SR, 4 hits
SUPFAMiSSF56487, SSF56487, 4 hits
PROSITEiView protein in PROSITE
PS00926, LYSYL_OXIDASE, 1 hit
PS00420, SRCR_1, 2 hits
PS50287, SRCR_2, 4 hits

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLOXL2_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9Y4K0
Secondary accession number(s): B2R5Q0
, Q53HV3, Q9BW70, Q9Y5Y8
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1999
Last modified: May 25, 2022
This is version 194 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families
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